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Structure paper

TitleA phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis.
Journal, issue, pagesBiochemistry, Vol. 52, Page 1603-1610, Year 2013
Publish dateFeb 8, 2013 (structure data deposition date)
AuthorsLiu, C.F. / Liu, D. / Momb, J. / Thomas, P.W. / Lajoie, A. / Petsko, G.A. / Fast, W. / Ringe, D.
External linksBiochemistry / PubMed:23387521
MethodsX-ray diffraction
Resolution1.45 - 1.72 Å
Structure data

PDB-4j5f:
Crystal Structure of B. thuringiensis AiiA mutant F107W
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-4j5h:
Crystal Structure of B. thuringiensis AiiA mutant F107W with N-decanoyl-L-homoserine bound at the active site
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-1K4:
N-decanoyl-L-homoserine

Source
  • bacillus thuringiensis (bacteria)
KeywordsHYDROLASE / AiiA / lactonase / dizinc hydrolase / substrate specificity / quorum quenching / beta-hairpin loops / N-acyl homoserine lactone / Hydrolase/Hydrolase substrate / Hydrolase-Hydrolase substrate complex

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